Research workbench
ARNT/HIF transcription FACTOR/COACTIVATOR complex
Analyse ARNT/HIF transcription FACTOR/COACTIVATOR complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PKY
- Type
- protein
- Length
- 497 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aryl hydrocarbon receptor nuclear translocator; Transforming acidic…
- UniProt
- P27540, Q9JJ11, Q99814
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 6 distinct chains · 49% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aryl hydrocarbon receptor nuclear translocator | protein | 101 | 28% helix, 43% strand | P27540 |
| B, F | Transforming acidic coiled-coil-containing protein 3 | protein | 49 | 96% helix, 0% strand | Q9JJ11 |
| C | Transforming acidic coiled-coil-containing protein 3 | protein | 47 | 96% helix, 0% strand | Q9JJ11 |
| D | Aryl hydrocarbon receptor nuclear translocator | protein | 101 | 30% helix, 43% strand | P27540 |
| E | Transforming acidic coiled-coil-containing protein 3 | protein | 50 | 94% helix, 0% strand | Q9JJ11 |
| G | Endothelial pas domain-containing protein 1 | protein | 100 | 22% helix, 39% strand | Q99814 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 542 | 0.67 | 0.78 | 62 | empty |
| 2 | 218 | 0.48 | 0.75 | 32 | empty |
| 3 | 90 | 0.38 | 0.76 | 15 | empty |
| 4 | 56 | 0.38 | 0.80 | 12 | empty |
| 5 | 52 | 0.31 | 0.77 | 11 | empty |
Interfaces
12 interfaces between chains.
- E–F · 1202 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 1190 Ų buried · 3 hydrogen bonds · protein-protein
- C–F · 864 Ų buried · 1 hydrogen bond · protein-protein
- B–G · 583 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 576 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4PKY · ARNT/HIF transcription factor/coactivator complex · the same entry in another collection · chain C against C, TM-score 1.00
- P27540 · AlphaFold monomer V2.0 prediction for aryl hydrocarbon receptor nuclear translocator… · a predicted model of the same protein · chain D against A, TM-score 0.99
- Q99814 · AlphaFold monomer V2.0 prediction for endothelial pas domain- containing protein 1… · a predicted model of the same protein · chain G against A, TM-score 0.98
- Q9JJ11 · AlphaFold monomer V2.0 prediction for transforming acidic coiled- coil-containing protein… · a predicted model of the same protein · chain C against A, TM-score 0.95
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P27540
- Every structure of UniProt Q9JJ11
- Every structure of UniProt Q99814
- Elsewhere: RCSB PDB 4PKY · PDBe 4PKY · UniProt P27540 · UniProt Q9JJ11 · UniProt Q99814
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